wave nucleic acid fragment analysis system Search Results


wave nucleic acid fragment analysis system  (ADS Biotec)
92
ADS Biotec wave nucleic acid fragment analysis system
Wave Nucleic Acid Fragment Analysis System, supplied by ADS Biotec, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 1 article reviews
wave nucleic acid fragment analysis system - by Bioz Stars, 2026-05
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wave 3500ht system  (ADS Biotec)
90
ADS Biotec wave 3500ht system
Wave 3500ht System, supplied by ADS Biotec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
wave 3500ht system - by Bioz Stars, 2026-05
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wave® nucleic acid fragment analysis system hsm  (Transgenomic)
90
Transgenomic wave® nucleic acid fragment analysis system hsm
Wave® Nucleic Acid Fragment Analysis System Hsm, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
wave® nucleic acid fragment analysis system hsm - by Bioz Stars, 2026-05
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wave hplc nucleic acid fragment analysis system  (Transgenomic)
90
Transgenomic wave hplc nucleic acid fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Wave Hplc Nucleic Acid Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wave hplc nucleic acid fragment analysis system/product/Transgenomic
Average 90 stars, based on 1 article reviews
wave hplc nucleic acid fragment analysis system - by Bioz Stars, 2026-05
90/100 stars
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automated wavetm nucleic acid fragment analysis system  (Transgenomic)
90
Transgenomic automated wavetm nucleic acid fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Automated Wavetm Nucleic Acid Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/automated wavetm nucleic acid fragment analysis system/product/Transgenomic
Average 90 stars, based on 1 article reviews
automated wavetm nucleic acid fragment analysis system - by Bioz Stars, 2026-05
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wave 2100a apparatus  (Transgenomic)
90
Transgenomic wave 2100a apparatus
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Wave 2100a Apparatus, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wave 2100a apparatus/product/Transgenomic
Average 90 stars, based on 1 article reviews
wave 2100a apparatus - by Bioz Stars, 2026-05
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high-performance liquid chromatography transgenomic wave nucleic acid high sensitivity fragment analysis system  (Transgenomic)
90
Transgenomic high-performance liquid chromatography transgenomic wave nucleic acid high sensitivity fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
High Performance Liquid Chromatography Transgenomic Wave Nucleic Acid High Sensitivity Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/high-performance liquid chromatography transgenomic wave nucleic acid high sensitivity fragment analysis system/product/Transgenomic
Average 90 stars, based on 1 article reviews
high-performance liquid chromatography transgenomic wave nucleic acid high sensitivity fragment analysis system - by Bioz Stars, 2026-05
90/100 stars
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wave nucleic acid fragment analysis system  (WaveMaker Software Inc)
90
WaveMaker Software Inc wave nucleic acid fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Wave Nucleic Acid Fragment Analysis System, supplied by WaveMaker Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wave nucleic acid fragment analysis system/product/WaveMaker Software Inc
Average 90 stars, based on 1 article reviews
wave nucleic acid fragment analysis system - by Bioz Stars, 2026-05
90/100 stars
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automated dhplc instrument wave nucleic acid fragment analysis system  (Transgenomic)
90
Transgenomic automated dhplc instrument wave nucleic acid fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Automated Dhplc Instrument Wave Nucleic Acid Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/automated dhplc instrument wave nucleic acid fragment analysis system/product/Transgenomic
Average 90 stars, based on 1 article reviews
automated dhplc instrument wave nucleic acid fragment analysis system - by Bioz Stars, 2026-05
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wave nucleic acid fragment analysis system hsm device  (WaveMaker Software Inc)
90
WaveMaker Software Inc wave nucleic acid fragment analysis system hsm device
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Wave Nucleic Acid Fragment Analysis System Hsm Device, supplied by WaveMaker Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wave nucleic acid fragment analysis system hsm device/product/WaveMaker Software Inc
Average 90 stars, based on 1 article reviews
wave nucleic acid fragment analysis system hsm device - by Bioz Stars, 2026-05
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automated dhplc instrumentation, the transgenomics wave nucleic acid fragment analysis system  (Transgenomic)
90
Transgenomic automated dhplc instrumentation, the transgenomics wave nucleic acid fragment analysis system
A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
Automated Dhplc Instrumentation, The Transgenomics Wave Nucleic Acid Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/automated dhplc instrumentation, the transgenomics wave nucleic acid fragment analysis system/product/Transgenomic
Average 90 stars, based on 1 article reviews
automated dhplc instrumentation, the transgenomics wave nucleic acid fragment analysis system - by Bioz Stars, 2026-05
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A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.

Journal: Open Biology

Article Title: Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile

doi: 10.1098/rsob.160272

Figure Lengend Snippet: A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.

Article Snippet: For the denaturing HPLC analyses, a gradient 0–8.8% v/v acetonitrile over 16 min was used to obtain optimal separation of primer products and ssDNA templates on a WAVE HPLC nucleic acid fragment analysis system equipped with a DNA Sep HPLC column (Transgenomic; Omaha, NE, USA).

Techniques: Residue, Binding Assay, Sequencing, High Performance Liquid Chromatography, Activity Assay, Mutagenesis, Synthesized